The effects of thermal treatment on emulsifying properties of soy protein isolates: Interfacial rheology and quantitative proteomic analysis

Shen, Qian; Xiong, Ting; Zheng, Wei; Luo, Yilun; Peng, Wei-Ting; Dai, Jun; Song, Rong; Li, Yan; Liu, Shilin; Li, Bin; Chen, Yijie

doi:10.1016/j.foodres.2022.111326

Cited by 16 publications

(4 citation statements)

References 45 publications

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“…26 Higher protein content was equivalent to higher concentration, which meant more protein was adsorbed onto the oil-water interface and reduced the interfacial tension. 27 The lower interfacial tension of ISF S , ISF SA and ISF SE compared with ISF U , ISF A and ISF E could be associated with the complex effect of an increased proportion of soluble dietary fiber and protein unfolding after steam explosion and enzymatic hydrolysis. The main component of soluble dietary fiber, soluble soybean polysaccharides, as a surface-active polysaccharide could reduce interfacial tension effectively.…”

Section: Soft Matter Papermentioning

confidence: 99%

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Preparation and characterization of emulsion gels stabilized by adequately preprocessed insoluble soybean fiber from okara

Huang

Cai

et al. 2023

Soft Matter

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Section: Soft Matter Papermentioning

confidence: 99%

“…A similar phenomenon of enhanced interface activity due to protein unfolding was also observed in the soy protein isolate after thermal treatment. 27 3.1.4. Emulsion properties.…”

Section: Soft Matter Papermentioning

confidence: 99%

Preparation and characterization of emulsion gels stabilized by adequately preprocessed insoluble soybean fiber from okara

Huang

Cai

et al. 2023

Soft Matter

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“…Therefore, hydrophobic and positively charged amino acid residues are the potential sites interacting with the interface. After the adsorption of proteins at the interface, changes are achieved not only quantitatively but also conformationally [ 7 , 8 ].…”

Section: Introductionmentioning

confidence: 99%

The Conformational Changes of Bovine Serum Albumin at the Air/Water Interface: HDX-MS and Interfacial Rheology Analysis

Han

Shen

Zheng

et al. 2023

Foods

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The characterization and dynamics of protein structures upon adsorption at the air/water interface are important for understanding the mechanism of the foamability of proteins. Hydrogen–deuterium exchange, coupled with mass spectrometry (HDX-MS), is an advantageous technique for providing conformational information for proteins. In this work, an air/water interface, HDX-MS, for the adsorbed proteins at the interface was developed. The model protein bovine serum albumin (BSA) was deuterium-labeled at the air/water interface in situ for different predetermined times (10 min and 4 h), and then the resulting mass shifts were analyzed by MS. The results indicated that peptides 54–63, 227–236, and 355–366 of BSA might be involved in the adsorption to the air/water interface. Moreover, the residues L55, H63, R232, A233, L234, K235, A236, R359, and V366 of these peptides might interact with the air/water interface through hydrophobic and electrostatic interactions. Meanwhile, the results showed that conformational changes of peptides 54–63, 227–236, and 355–366 could lead to structural changes in their surrounding peptides, 204–208 and 349–354, which could cause the reduction of the content of helical structures in the rearrangement process of interfacial proteins. Therefore, our air/water interface HDX-MS method could provide new and meaningful insights into the spatial conformational changes of proteins at the air/water interface, which could help us to further understand the mechanism of protein foaming properties.

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“…Soy protein isolate contains more than 90% protein, nearly 20 kinds of amino acids and human essential amino acids. Its nutrient‐rich, cholesterol‐free, soy protein isolate is one of the few alternatives to animal protein varieties (Shen et al, 2022 ; Zhang et al, 2022 ). Because of its good surface activity, it can reduce the surface tension of water and oil and reduce the surface tension of water and air, and it easily forms a stable emulsion; therefore, soy protein isolate is widely used in food (Du et al, 2022 ; Ma et al, 2022 ).…”

Section: Introductionmentioning

confidence: 99%

Modulation of physicochemical properties of lipid droplets using soy protein isolate and lactoferrin interfacial coatings

Zhang,

Du,

2023

Food Science & Nutrition

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In order to improve the physicochemical stability of soy protein isolate (SPI) emulsion, lactoferrin (LF) was used to modify the interface layer. The stable multilayer emulsion can be formed when the content of lactoferrin is 0.5% at pH 5. The emulsion with good stability was at pH 3–7, and it was also stable to temperature change. The FFAs release of SPI emulsion and LF‐SPI emulsion was 103.9% and 103.7%, respectively. The results showed that the lactoferrin layer did not hinder the digestion of oil and the bioaccessibility of carotenoids, but lactoferrin layer improved the physicochemical stability of SPI emulsions. This work provides information valuable in the design of emulsion formulations for applications in the food, pharmaceutical, and personal care industries.

show abstract

The effects of thermal treatment on emulsifying properties of soy protein isolates: Interfacial rheology and quantitative proteomic analysis

Cited by 16 publications

References 45 publications

Preparation and characterization of emulsion gels stabilized by adequately preprocessed insoluble soybean fiber from okara

Preparation and characterization of emulsion gels stabilized by adequately preprocessed insoluble soybean fiber from okara

The Conformational Changes of Bovine Serum Albumin at the Air/Water Interface: HDX-MS and Interfacial Rheology Analysis

Modulation of physicochemical properties of lipid droplets using soy protein isolate and lactoferrin interfacial coatings

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